Last Updated: 24/02/2025
Elucidation of novel secretion mechanism independent of endoplasmic reticulum signal peptide in protozoa
Objectives
*Original title and text were machine translated from Japanese.
The research investigates a novel secretion mechanism in protozoa that operates independently of endoplasmic reticulum signal peptides, focusing on the role of PfArf1 GTPase and its myristoylation modification in extracellular protein transport.
The N-terminus signal peptide of secreted proteins is required for the protein to be transported out of the endoplasmic reticulum. However, several secreted proteins without a signal peptide have been reported in protozoa and host cells. In this study, Nakano showed that EhTolA is transported to the cell surface by the endoplasmic reticulum-localized Rab8A GTPase in Entamoeba histolytica. N-terminal myristylation modification of EhTolA was necessary for transport to the amebic cell surface. In addition, myristoylated PfRab5b GTPase, which is localized to the ER, is involved in the transport of myristoylated substrate, AK2, to the parasitophorous vacuolar membrane in Plasmodium falciparum. The regulatory factors involved in the regulation of PfRab5b were also analyzed.
Apr 2019 — Mar 2023
$37,260
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